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Merck

S4826

SMIFH2

≥98% (HPLC), actin assembly inhibitor, powder

Sinónimos:

1-(3-Bromophenyl)-5-(2-furanylmethylene)dihydro-2-thioxo-4,6(1H,5H)-pyrimidinedione

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Fórmula empírica (notación de Hill):
C15H9BrN2O3S
Número CAS:
340316-62-3
Peso molecular:
377.21
UNSPSC Code:
12352200
NACRES:
NA.77
Assay:
≥98% (HPLC)
Form:
powder
Quality level:
100
Storage condition:
protect from light

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Nombre del producto

SMIFH2, ≥98% (HPLC)

SMILES string

S=C1N(C(=O)\C(=C\c3[o]ccc3)\C(=O)N1)c2cc(ccc2)Br

InChI

1S/C15H9BrN2O3S/c16-9-3-1-4-10(7-9)18-14(20)12(13(19)17-15(18)22)8-11-5-2-6-21-11/h1-8H,(H,17,19,22)/b12-8+

InChI key

MVFJHEQDISFYIS-XYOKQWHBSA-N

assay

≥98% (HPLC)

form

powder

storage condition

protect from light

color

light yellow to yellow-green

solubility

DMSO: 20 mg/mL, clear

storage temp.

2-8°C

Quality Level

100

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Categorías relacionadas

Application

SMIFH2 was used to decipher the role of mDia2 in controlling microtubule dynamics and myofibroblast differentiation.1

Biochem/physiol Actions

SMIFH2 is an inhibitor of formin homology 2 domains. The compound is a first small molecule inhibitor of formin-mediated actin assembly that disrupts formin dependent processes from yeast to mammals. SMIFH2 may be a useful drug for identifying cellular processes dependent on formin-mediated actin assembly in a broad range of experimental systems. Formin is an actin nucleation factor.
SMIFH2 is an inhibitor of formin-mediated actin assembly that disrupts formin dependent processes.

Clase de almacenamiento

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificados de análisis (COA)

Lot/Batch Number
076M4606V
075M4601V
113M4609V
080M4605

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Chang Liu et al.
Molecular plant, 11(11), 1389-1399 (2018-10-09)
The process of pollen germination is crucial for flowering plant reproduction, but the mechanisms through which pollen grains establish polarity and select germination sites are not well understood. In this study, we report that a formin family protein, AtFH5, is localized
Anushree C Gulvady et al.
Molecular biology of the cell, 30(11), 1298-1313 (2019-03-21)
Fibroblasts transformed by the proto-oncogene Src form individual invadopodia that can spontaneously self-organize into large matrix-degrading superstructures called rosettes. However, the mechanisms by which the invadopodia can spatiotemporally reorganize their architecture is not well understood. Here, we show that Hic-5
N O Alieva et al.
Nature communications, 10(1), 3593-3593 (2019-08-11)
Filopodia, dynamic membrane protrusions driven by polymerization of an actin filament core, can adhere to the extracellular matrix and experience both external and cell-generated pulling forces. The role of such forces in filopodia adhesion is however insufficiently understood. Here, we
Michael Keegan Delaney et al.
Proceedings of the National Academy of Sciences of the United States of America, 114(33), E6932-E6941 (2017-08-02)
Diaphanous (Dia)-related formins (DRFs) coordinate cytoskeletal remodeling by controlling actin nucleation and microtubule (MT) stabilization to facilitate processes such as cell polarization and migration; yet the full extent of their activities remains unknown. Here, we uncover two discrete roles and
Sarah J Copeland et al.
Molecular biology of the cell, 29(13), 1611-1627 (2018-05-10)
A primary cilium is found on most mammalian cells, where it acts as a cellular antenna for the reception of both mechanical and chemical signals. A variety of diseases are associated with defective ciliogenesis, reflecting the ubiquity of the function
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